Substitution of Arginine 719 for Glutamic Acid in Human Plasminogen Substantially Reduces Its Affinity for Streptokinase

In isolation human plasminogen possesses no enzymatic activity, yet upon formation of an equimolar complex with the bacterial protein streptokinase, it acquires a plasminogen activator function. The region(s) of plasminogen and of streptokinase which mediate complex formation has (have) not been pre...

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Veröffentlicht in:	Biochemistry (Easton) 1994-10, Vol.33 (40), p.12042-12047
Hauptverfasser:	Dawson, Keith M, Marshall, Julian M, Raper, Robert H, Gilbert, Richard J, Ponting, Christopher P
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antibodies, Monoclonal Arginine - chemistry Base Sequence Binding Sites CHO Cells Chromatography, High Pressure Liquid Cricetinae Enzyme-Linked Immunosorbent Assay Glutamic Acid - chemistry Humans Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Oligonucleotides - chemistry Plasminogen - chemistry Plasminogen - genetics Plasminogen - metabolism Plasminogen Activators Protein Conformation Recombinant Proteins - chemistry Recombinant Proteins - metabolism Serine Endopeptidases - metabolism Streptokinase - metabolism
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